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The structure of bovine mitochondrial F1-ATPase: an example of rotary catalysis
A G Leslie1, J P Abrahams, K Braig
1MRC Laboratory of Molecular Biology, Cambridge, U.K.
Biochemical Society Transactions
|March 27, 1999
Abstract:
There is now compelling evidence in support of a rotary catalytic mechanism in F1-ATPase, and, by extension, in the intact ATP synthase. Although models have been proposed to explain how protein translocation in F0 results in rotation of the gamma-subunit relative to the alpha 3/beta 3 assembly in F1 [22], these are still speculative. It seems likely that a satisfactory explanation of this mechanism will ultimately depend on structural information on the intact ATP synthase.